W3L2 - Macromolecules II - Proteins Flashcards

(21 cards)

1
Q

What is the structure of proteins

A

polymers (many molecules) of amino acid monomers

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2
Q

What are the polymers of amino acids also referred to as

A

polypeptides

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3
Q

How are amino acids linked together

A

by peptide bonds

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4
Q

Describe the primary structure of a protein

A

Long linear sequence of amino acids joined by peptide bonds

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5
Q

what are the two major elements of a secondary protein

A

alpha-helix and beta strand

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6
Q

What do bonds do secondary proteins have?

A

hydrogen bonding

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7
Q

What are the regions that allow changes in the direction of the polypeptide chain

A

turns and loops

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8
Q

Why do you need turn and loops within a protein

A

proper folding determines how a protein works in the body

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9
Q

In what directions can beta sheets in secondary structures form

A

parallel and anti-parallel

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10
Q

What are the weak interactions that contribute to the structure of the tertiary protein

A

hydrophobic interaction, hydrogen bonding, ionic bonds

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11
Q

If the tertiary protein has these weak interactions why is the overall protein still strong

A

individually the forces are weak but when combined together they form an overall strong structure

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12
Q

What are the strongest bonds within a tertiary protein structure

A

disulfide bridges

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13
Q

What is the feature of a fibrous 3D protein structures (tertiary) protein structure?

A

long, rod-like, insoluble in water, mostly alpha-helices

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14
Q

What are examples of fibrous 3D protein structures?

A

collagen (tendons, ligaments), fibroin (spider silk), keratin (hair, nails), fibrin (blood clot)

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15
Q

Explain the features of a globular 3D protein structures

A

compact + fold back on themselves, usually soluble, complex structures, both alpha-helices and beta sheets

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16
Q

Examples of a globular 3D protein structures

17
Q

What is the structure of quaternary protein structures

A

consisting of more than one polypeptide chain

18
Q

What is protein denaturation

A

conditions (pH/heat) → disrupt secondary/tertiary structure of a protein → lose function

19
Q

What is the function of enzymatic proteins

A

selective acceleration of chemical reactions

20
Q

What is an example of enzymatic proteins

A

digestive enzymes catalyse the hydrolysis of bonds in food molecules (break down)

21
Q

What is the primary function of proteins

A

enzymal activity